Dr Muhammad Fairuz Jamaluddin

Dr Muhammad Fairuz Jamaluddin

Research Assistant

School of Biomedical Sciences and Pharmacy

Career Summary

Biography

Dr Fairuz Jamaluddin is an early career researcher who is developing expertise in gynaecology oncology. He was recently awarded with John Hunter Hospital Charitable Trust project grant (3x) since 2017 to advance his project. He independently pursued his own research project on the molecular basis of uterine fibroids, ovarian cancer and endometrial cancer, combining human genetics and mass spectrometry-based proteomics.

Dr Fairuz Jamaluddin graduated his PhD in 2015 at the University of Queensland. During his doctoral studies, he learnt and developed new methodologies in glycoproteomics in Associate Professor Benjamin Schulz’s lab. In 2016, he joined the Gynaecology Oncology Research Group of Associate Professor Pradeep Tanwar (NHMRC fellow and international leader on gynaecological cancer research) as a Postdoctoral Researcher in the School of Biomedical Sciences and Pharmacy, University of Newcastle.  Dr Jamaluddin has published in high impact journals including Molecular and Cellular Proteomics x2, Nature Communications, Cell Reports and Carcinogenesis. In particular, his work with Assoc Prof Tanwar is the first study in the field to characterise the matrisome of uterine fibroids and identified the key biomarkers of this disease development in genetically annotated patient samples (Endocrinology 2018). This work led to ‘Publication of the Month May 2018’ awarded by the School of Biomedical Science and Pharmacy. Dr Jamaluddin pioneering work also identified two novel ECM proteins namely periostin (Endocrinology 2018) and tenascin-C (Reproductive Science 2019) that are upregulated in fibroid patients. He is also one of the co-authors involved in investigating the mechanistic insight how changes in ECM and its biomechanical properties leads to overactivation of canonical Wnt/β-catenin signalling (Reproduction 2018). Based on his outstanding contributions to the field, he was recently awarded with ‘Kellerman Award 2019’ by the Faculty of Health and Medicine.

Research Focus

Dr Fairuz Jamaluddin research is focused on discovering new ways of detecting and treating diseases of the female reproductive tract including endometriosis, fibroids, ovarian cancer and endometrial cancer. Dr Jamaluddin is interested in applying mass spectrometry-based proteomics as a powerful tool to study protein profiles of diseased and normal tissues. By comparing protein profiles of diseased and normal tissues, new protein biomarkers for early diagnosis or developing new drug treatments can be uncovered.

His current research addresses three main areas:

- Targeting extracellular matrix as therapeutic approach in uterine leiomyoma (fibroids)

- New drug targets for ovarian cancer metastasis and drug resistance

- Disease biomarkers for early detection of endometriosis and endometrial cancer


Qualifications

  • Doctor of Philosophy, University of Queensland

Keywords

  • Extracellular matrix
  • Medical Biochemistry
  • Proteomics

Languages

  • English (Fluent)
  • Malay (Mother)

Fields of Research

Code Description Percentage
111201 Cancer Cell Biology 50
110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics) 20
111203 Cancer Genetics 30

Professional Experience

Academic appointment

Dates Title Organisation / Department
1/2/2017 - 31/1/2018 Lecturer School of Biomedical Sciences and Pharmacy, Faculty of Health and Medicine, University of Newcastle
Australia

Awards

Award

Year Award
2019 The Kellerman Award
Faculty of Health and Medicine, University of Newcastle

Prize

Year Award
2018 Publication of the Month May
Faculty of Health and Medicine, University of Newcastle

Teaching

Code Course Role Duration
HUBS3409 Projects in Biomedical Science
School of Biomedical Sciences and Pharmacy, Faculty of Health and Medicine, University of Newcastle

This course provide an opportunity for students to study a current field of research in biomedical science in greater depth and to gain the intellectual and professional skills associated with managing, implementing and reporting on a biomedical research project. The assessment on student performance in this course is based on their literature review, project seminar, project manuscript and supervisors report.

 

Teaching 1/2/2017 - 31/1/2018
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Publications

For publications that are currently unpublished or in-press, details are shown in italics.


Chapter (1 outputs)

Year Citation Altmetrics Link
2019 Gould T, Jamaluddin M, Petit J, King SJ, Nixon B, Scott R, et al., 'Finding Needles in Haystacks: The Use of Quantitative Proteomics for the Early Detection of Colorectal Cancer', Advances in the Molecular Understanding of Colorectal Cancer, IntechOpen, Switzerland 1-32 (2019) [B1]
DOI 10.5772/intechopen.80942
Co-authors Peter Pockney, Matt Dun, Rodney Scott, Brett Nixon

Journal article (15 outputs)

Year Citation Altmetrics Link
2020 Ferdoushi A, Li X, Jamaluddin MFB, Hondermarck H, 'Front Cover: Proteomic Profile of Human Schwann Cells', PROTEOMICS, 20 2070001-2070001 (2020)
DOI 10.1002/pmic.202070001
2020 Ali A, Syed SM, Jamaluddin MFB, Colino-Sanguino Y, Gallego-Ortega D, Tanwar PS, 'Cell Lineage Tracing Identifies Hormone-Regulated and Wnt-Responsive Vaginal Epithelial Stem Cells', Cell Reports, 30 1463-1477.e7 (2020)

© 2020 The Authors The intact vaginal epithelium is essential for women's reproductive health and provides protection against HIV and sexually transmitted infections. How thi... [more]

© 2020 The Authors The intact vaginal epithelium is essential for women's reproductive health and provides protection against HIV and sexually transmitted infections. How this epithelium maintains itself remains poorly understood. Here, we used single-cell RNA sequencing (RNA-seq) to define the diverse cell populations in the vaginal epithelium. We show that vaginal epithelial cell proliferation is limited to the basal compartment without any obvious label-retaining cells. Furthermore, we developed vaginal organoids and show that the basal cells have increased organoid forming efficiency. Importantly, Axin2 marks a self-renewing subpopulation of basal cells that gives rise to differentiated cells over time. These cells are ovariectomy-resistant stem cells as they proliferate even in the absence of hormones. Upon hormone supplementation, these cells expand and reconstitute the entire vaginal epithelium. Wnt/ß-catenin is essential for the proliferation and differentiation of vaginal stem cells. Together, these data define heterogeneity in vaginal epithelium and identify vaginal epithelial stem cells.

DOI 10.1016/j.celrep.2020.01.003
Co-authors Pradeep Tanwar
2019 Ferdoushi A, Li X, Bin Jamaluddin MF, Hondermarck H, 'Proteomic Profile of Human Schwann Cells', PROTEOMICS, 20 (2019)
DOI 10.1002/pmic.201900294
Co-authors Hubert Hondermarck
2019 Nixon B, De Iuliis GN, Hart HM, Zhou W, Mathe A, Bernstein IR, et al., 'Proteomic profiling of mouse epididymosomes reveals their contributions to post-testicular sperm maturation', Molecular and Cellular Proteomics, 18 S91-S108 (2019) [C1]
DOI 10.1074/mcp.RA118.000946
Citations Scopus - 13Web of Science - 18
Co-authors Brett Nixon, Matt Dun, Elizabeth Bromfield, David Skerrett-Byrne, Geoffry DeiuliIs, Andrea Johns
2019 Al-Juboori AAA, Ghosh A, Bin Jamaluddin MF, Kumar M, Sahoo SS, Syed SM, et al., 'Proteomic Analysis of Stromal and Epithelial Cell Communications in Human Endometrial Cancer Using a Unique 3D Co-Culture Model', PROTEOMICS, 19 (2019) [C1]
DOI 10.1002/pmic.201800448
Citations Scopus - 1Web of Science - 1
Co-authors Manishkumar Jhamb, Pradeep Tanwar
2019 Jamaluddin MFB, Nagendra PB, Nahar P, Oldmeadow C, Tanwar PS, 'Proteomic Analysis Identifies Tenascin-C Expression Is Upregulated in Uterine Fibroids', REPRODUCTIVE SCIENCES, 26 476-486 (2019) [C1]
DOI 10.1177/1933719118773420
Citations Scopus - 3Web of Science - 1
Co-authors Christopher Oldmeadow, Pradeep Tanwar
2018 Goad J, Ko Y-A, Kumar M, Jamaluddin MFB, Tanwar PS, 'Oestrogen fuels the growth of endometrial hyperplastic lesions initiated by overactive Wnt/ß-catenin signalling.', Carcinogenesis, 39 1105-1116 (2018) [C1]
DOI 10.1093/carcin/bgy079
Citations Scopus - 2Web of Science - 2
Co-authors Pradeep Tanwar, Manishkumar Jhamb
2018 Ko YA, Jamaluddin MFB, Adebayo M, Bajwa P, Scott RJ, Dharmarajan AM, et al., 'Extracellular matrix (ECM) activates ß-catenin signaling in uterine fibroids', Reproduction, 155 61-71 (2018) [C1]

© 2018 Society for Reproduction and Fertility. Recent studies showed that genetic aberrations in the MED12 gene, probably through the canonical WNT/ß-catenin pathway, lead to the ... [more]

© 2018 Society for Reproduction and Fertility. Recent studies showed that genetic aberrations in the MED12 gene, probably through the canonical WNT/ß-catenin pathway, lead to the pathogenesis of uterine fibroids. However, a comprehensive analysis of the WNT pathway in MED12-mutated and MED12-wildtype fibroids has not been performed. The objective of this study was to determine the status of the WNT pathway in human fibroids. We performed Sanger sequencing to define the MED12 mutational status of fibroids and normal myometrium samples. qPCR arrays were carried out to determine the status of the WNT signaling pathway in MED12-mutated and MED12-wild-type fibroids. Liquid chromatography-mass spectrometry (LC-MS), Western blotting and immunohistochemistry were used to monitor the expression of ß-catenin. We showed that ß-catenin expression was increased in fibroids compared to the adjacent myometrium samples. However, ß-catenin expression showed no correlation with MED12 mutation status. Of all the WNT signaling components, WNT inhibitors showed the greatest differences in expression between fibroids and controls. WIF1, a WNT inhibitor, was identified as the most significantly upregulated gene in fibroids. We cultured primary fibroid cells on hydrogels of known stiffness to decipher the influence of biomechanical cues on ß-catenin expression and revealed increased levels of ß-catenin when cells were cultured on a stiffer surface. In conclusion, our data showed that ß-catenin expression in fibroids occurs independently of MED12 mutations. Biomechanical changes upregulate ß-catenin expression in fibroids, providing an attractive avenue for developing new treatments for this disease.

DOI 10.1530/REP-17-0339
Citations Scopus - 6Web of Science - 8
Co-authors Rodney Scott, Pradeep Tanwar
2018 Jamaluddin MFB, Nahar P, Tanwar PS, 'Proteomic characterization of the extracellular matrix of human uterine fibroids', Endocrinology, 159 2656-2669 (2018) [C1]

© 2018 Endocrine Society. Uterine leiomyomas (fibroids) are the most common benign tumors that are associated with increased production of extracellular matrix (ECM). Excessive EC... [more]

© 2018 Endocrine Society. Uterine leiomyomas (fibroids) are the most common benign tumors that are associated with increased production of extracellular matrix (ECM). Excessive ECM deposition plays a major role in the enlargement and stiffness of these tumors and contributes to clinical symptoms, such as abnormal bleeding and abdominal pain. However, no study so far has explored the global composition of the ECM of fibroids and normal myometrium. In this study, we performed a systematic ECM enrichment procedure and comparative proteomic analyses to profile the ECM composition of genetically annotated different-sized fibroids (small, medium, and large) and adjacent normal myometrium (ANM). Our matrisome analysis identified a combined total of 108, 126, 126, and 130 unique ECM and ECM-associated proteins with a confidence corresponding to a false discovery rate,1%inANM and in small, medium, and large fibroids, respectively. The majority of fibroid ECM proteins belong to the core matrisome that includes glycoproteins, collagens, and proteoglycans. Considering that the small-sized fibroids represent the initial stages of leiomyogenesis, we highlighted some of the most abundant and important upregulated ECM proteins in small fibroids (i.e., POSTN, TNC, COL3A1, COL24A1, and ASPN). Furthermore, we revealed 30 unique ECM proteins that exist only in fibroids but that are not present in ANM regardless of MED12 mutation. We propose that some of the proteins identified represent potential novel ECM drug targets that may change the paradigm of fibroid treatment.

DOI 10.1210/en.2018-00151
Citations Scopus - 5Web of Science - 7
Co-authors Pradeep Tanwar
2018 Jamaluddin MFB, Ko YA, Kumar M, Brown Y, Bajwa P, Nagendra PB, et al., 'Proteomic profiling of human uterine fibroids reveals upregulation of the extracellular matrix protein periostin', Endocrinology, 159 1106-1118 (2018) [C1]

Copyright © 2018 Endocrine Society The central characteristic of uterine fibroids is excessive deposition of extracellular matrix (ECM), which contributes to fibroid growth and bu... [more]

Copyright © 2018 Endocrine Society The central characteristic of uterine fibroids is excessive deposition of extracellular matrix (ECM), which contributes to fibroid growth and bulk-type symptoms. Despite this, very little is known about patterns of ECM protein expression in fibroids and whether these are influenced by the most common genetic anomalies, which relate to MED12. We performed extensive genetic and proteomic analyses of clinically annotated fibroids and adjacent normal myometrium to identify the composition and expression patterns of ECM proteins in MED12 mutation-positive and mutation-negative uterine fibroids. Genetic sequencing of tissue samples revealed MED12 alterations in 39 of 65 fibroids (60%) from 14 patients. Using isobaric tagged-based quantitative mass spectrometry on three selected patients (n = 9 fibroids), we observed a common set of upregulated (.1.5-fold) and downregulated (,0.66-fold) proteins in small, medium, and large fibroid samples of annotated MED12 status. These two sets of upregulated and downregulated proteins were the same in all patients, regardless of variations in fibroid size and MED12 status. We then focused on one of the significant upregulated ECM proteins and confirmed the differential expression of periostin using western blotting and immunohistochemical analysis. Our study defined the proteome of uterine fibroids and identified that increased ECM protein expression, in particular periostin, is a hallmark of uterine fibroids regardless of MED12 mutation status. This study sets the foundation for further investigations to analyze the mechanisms regulating ECM overexpression and the functional role of upregulated ECM proteins in leiomyogenesis.

DOI 10.1210/en.2017-03018
Citations Scopus - 5Web of Science - 5
Co-authors Pradeep Tanwar, Manishkumar Jhamb, David Skerrett-Byrne, Matt Dun, Mark Baker, Hubert Hondermarck, Rodney Scott
2014 Jamaluddin MFB, Bailey UM, Schulz BL, 'Oligosaccharyltransferase subunits bind polypeptide substrate to locally enhance N-glycosylation', Molecular and Cellular Proteomics, 13 3286-3293 (2014)

© 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Oligosaccharyltransferase is a multiprotein complex that catalyzes asparagine-linked glycosylation of d... [more]

© 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Oligosaccharyltransferase is a multiprotein complex that catalyzes asparagine-linked glycosylation of diverse proteins. Using yeast genetics and glycoproteomics, we found that transient interactions between nascent polypeptide and Ost3p/Ost6p, homologous subunits of oligosaccharyltransferase, were able to modulate glycosylation efficiency in a site-specific manner in vivo. These interactions were driven by hydrophobic and electrostatic complementarity between amino acids in the peptidebinding groove of Ost3p/Ost6p and the sequestered stretch of substrate polypeptide. Based on this dependence, we used in vivo scanning mutagenesis and in vitro biochemistry to map the precise interactions that affect site-specific glycosylation efficiency. We conclude that transient binding of substrate polypeptide by Ost3p/Ost6p increases glycosylation efficiency at asparagines proximal and C-terminal to sequestered sequences. We detail a novel mode of interaction between translocating nascent polypeptide and oligosaccharyltransferase in which binding to Ost3p/Ost6p segregates a short flexible loop of glycosylation-competent polypeptide substrate that is delivered to the oligosaccharyltransferase active site for efficient modification.

DOI 10.1074/mcp.M114.041178
Citations Scopus - 10Web of Science - 10
2014 Tan NY, Bailey UM, Jamaluddin MF, Mahmud SHB, Raman SC, Schulz BL, 'Sequence-based protein stabilization in the absence of glycosylation', Nature Communications, 5 (2014)

Asparagine-linked N-glycosylation is a common modification of proteins that promotes productive protein folding and increases protein stability. Although N-glycosylation is import... [more]

Asparagine-linked N-glycosylation is a common modification of proteins that promotes productive protein folding and increases protein stability. Although N-glycosylation is important for glycoprotein folding, the precise sites of glycosylation are often not conserved between protein homologues. Here we show that, in Saccharomyces cerevisiae, proteins upregulated during sporulation under nutrient deprivation have few N-glycosylation sequons and in their place tend to contain clusters of like-charged amino-acid residues. Incorporation of such sequences complements loss of in vivo protein function in the absence of glycosylation. Targeted point mutation to create such sequence stretches at glycosylation sequons in model glycoproteins increases in vitro protein stability and activity. A dependence on glycosylation for protein stability or activity can therefore be rescued with a small number of local point mutations, providing evolutionary flexibility in the precise location of N-glycans, allowing protein expression under nutrient-limiting conditions, and improving recombinant protein production. © 2014 Macmillan Publishers Limited. All rights reserved.

DOI 10.1038/ncomms4099
Citations Scopus - 17Web of Science - 15
2013 Mohd Yusuf SNH, Bailey UM, Tan NY, Jamaluddin MF, Schulz BL, 'Mixed disulfide formation in vitro between a glycoprotein substrate and yeast oligosaccharyltransferase subunits Ost3p and Ost6p', Biochemical and Biophysical Research Communications, 432 438-443 (2013)

Oligosaccharyltransferase (OTase) glycosylates selected asparagine residues in secreted and membrane proteins in eukaryotes, and asparagine (N)-glycosylation affects the folding, ... [more]

Oligosaccharyltransferase (OTase) glycosylates selected asparagine residues in secreted and membrane proteins in eukaryotes, and asparagine (N)-glycosylation affects the folding, stability and function of diverse glycoproteins. The range of acceptor protein substrates that are efficiently glycosylated depends on the action of several accessory subunits of OTase, including in yeast the homologous proteins Ost3p and Ost6p. A model of Ost3p and Ost6p function has been proposed in which their thioredoxin-like active site cysteines form transient mixed disulfide bonds with cysteines in substrate proteins to enhance the glycosylation of nearby asparagine residues. We tested aspects of this model with a series of in vitro assays. We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p. A complementary peptide affinity chromatography assay for mixed disulfide bond formation showed that Ost3p could also form mixed disulfide bonds with cysteines in selected reduced tryptic peptides from Gas1p. Together, these assays showed that the thioredoxin-like active sites of Ost3p and Ost6p could form transient mixed disulfide bonds with cysteines in a model substrate glycoprotein, consistent with the function of Ost3p and Ost6p in modulating N-glycosylation substrate selection by OTase in vivo. © 2013 Elsevier Inc.

DOI 10.1016/j.bbrc.2013.01.128
Citations Scopus - 10Web of Science - 11
2012 Bailey U-M, Jamaluddin MF, Schulz BL, 'Analysis of Congenital Disorder of Glycosylation-Id in a Yeast Model System Shows Diverse Site-Specific Under-glycosylation of Glycoproteins', JOURNAL OF PROTEOME RESEARCH, 11 5376-5383 (2012)
DOI 10.1021/pr300599f
Citations Scopus - 35Web of Science - 35
2011 Jamaluddin MFB, Bailey U-M, Tan NYJ, Stark AP, Schulz BL, 'Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p', PROTEIN SCIENCE, 20 849-855 (2011)
DOI 10.1002/pro.610
Citations Scopus - 19Web of Science - 20
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Conference (7 outputs)

Year Citation Altmetrics Link
2019 Duchatel RJ, Jackson ER, Staudt D, Skerrett-Byrne DA, Jamaluddin MFB, Germon Z, et al., 'Keynote Speakers', ASIA-PACIFIC JOURNAL OF CLINICAL ONCOLOGY (2019)
DOI 10.1111/ajco.13253
Co-authors Matt Dun, David Skerrett-Byrne
2019 Brown Y, Ghosh A, Venkata VD, Jamaluddin MFB, Ali A, Tanwar PS, 'Enter the Matrix to Uncover Potential New Biomarkers for the Initial Stages of Ovarian Cancer Development', ASIA-PACIFIC JOURNAL OF CLINICAL ONCOLOGY (2019)
Co-authors Pradeep Tanwar
2019 Jamaluddin M, Ko Y-A, Syed S, Ius Y, O'Sullivan R, Netherton J, et al., 'Understanding the basis of intra-tumour heterogeneity in human endometrial cancer', Newcastle City Hall, Newcastle, NSW, Australia (2019)
Co-authors Mark Baker, Pradeep Tanwar
2018 Brown Y, Jamaluddin MFB, Ghosh A, Mellick AS, Murtha L, Boyle A, Tanwar PS, 'The Glue of Cancer Cell Life: Characterization of the Acellular Component of High Grade Serous Ovarian Cancer Identifies Potential Novel Drug Targets', ASIA-PACIFIC JOURNAL OF CLINICAL ONCOLOGY (2018)
Co-authors Lucy Murtha, Pradeep Tanwar
2018 Jamaluddin MFB, Ko Y-A, Ius Y, O'Sullivan R, Nahar P, Jaaback K, Tanwar PS, 'Why Targeted Therapies Don't Work?: Proteomic Characterization of Intratumor Heterogeneity of Human Endometrial Cancer', ASIA-PACIFIC JOURNAL OF CLINICAL ONCOLOGY (2018)
Co-authors Pradeep Tanwar
2018 Gould T, Jamaluddin MFB, Pockney P, Dun M, 'Quantitative Proteomics for the Early Detection of Colorectal Cancer', ASIA-PACIFIC JOURNAL OF CLINICAL ONCOLOGY (2018)
Co-authors Peter Pockney, Matt Dun
2017 Yi-An K, Jamaluddin M, Tanwar PS, 'Extracellular Matrix (ECM) and Wnt signalling nexus in human uterine leiomyomas', Perth (2017)
Co-authors Pradeep Tanwar
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Thesis / Dissertation (1 outputs)

Year Citation Altmetrics Link
2015 Jamaluddin M, Molecular mechanisms regulating N-glycosylation site selection by yeast oligosaccharyltransferase: Role of Ost3p and Ost6p, The University of Queensland (2015)
DOI 10.14264/uql.2015.362
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Grants and Funding

Summary

Number of grants 9
Total funding $829,870

Click on a grant title below to expand the full details for that specific grant.


20195 grants / $734,563

Defining the roles of hormones in the pathogenesis of ovarian cancer$566,277

Funding body: Ovarian Cancer Research Foundation (OCRF)

Funding body Ovarian Cancer Research Foundation (OCRF)
Project Team Associate Professor Pradeep Tanwar, Doctor Muhammad Fairuz Jamaluddin, Prof Arunasalam Dharmarajan
Scheme Research Grant
Role Investigator
Funding Start 2019
Funding Finish 2021
GNo G1900444
Type Of Funding C3112 - Aust Not for profit
Category 3112
UON Y

Endometrial Cancer Research Project$96,000

Funding body: Hunter Medical Research Institute

Funding body Hunter Medical Research Institute
Project Team Associate Professor Pradeep Tanwar, Doctor Shafiq Syed, Doctor Muhammad Fairuz Jamaluddin
Scheme Project Grant
Role Investigator
Funding Start 2019
Funding Finish 2019
GNo G1900346
Type Of Funding C3120 - Aust Philanthropy
Category 3120
UON Y

Microinjection workstation to facilitate disease modelling in organoids$47,862

Funding body: NHMRC (National Health & Medical Research Council)

Funding body NHMRC (National Health & Medical Research Council)
Project Team Associate Professor Pradeep Tanwar, Professor Xu Dong Zhang, Doctor Lei Jin, Professor Hubert Hondermarck, Associate Professor Susan Hua, Doctor Muhammad Fairuz Jamaluddin
Scheme Equipment Grant
Role Investigator
Funding Start 2019
Funding Finish 2019
GNo G1900304
Type Of Funding Scheme excluded from IGS
Category EXCL
UON Y

Proteomic characterization of human uterine fibroids harbouring co-existing MED12 and FH in Australian women$20,063

Funding body: John Hunter Hospital Charitable Trust

Funding body John Hunter Hospital Charitable Trust
Project Team Doctor Muhammad Fairuz Jamaluddin, Associate Professor Pradeep Tanwar, Doctor Pravin Nahar
Scheme Research Grant
Role Lead
Funding Start 2019
Funding Finish 2019
GNo G1900225
Type Of Funding C2220 - Aust StateTerritoryLocal - Other
Category 2220
UON Y

Temperature regulated incubator shaker$4,361

Funding body: Hunter Medical Research Institute

Funding body Hunter Medical Research Institute
Project Team Associate Professor Pradeep Tanwar, Doctor Mahesh Kumar, Doctor Muhammad Fairuz Jamaluddin
Scheme Early and Mid-Career Equipment Grant
Role Investigator
Funding Start 2019
Funding Finish 2019
GNo G1900105
Type Of Funding C3120 - Aust Philanthropy
Category 3120
UON Y

20183 grants / $75,307

Non-invasive detection of DIPG specific DNA and protein using sequential blood collections$38,000

Funding body: Hunter Medical Research Institute

Funding body Hunter Medical Research Institute
Project Team Doctor Matt Dun, Doctor Muhammad Fairuz Jamaluddin, Doctor Ryan Duchatel, Doctor Frank Alvaro
Scheme Project Grant
Role Investigator
Funding Start 2018
Funding Finish 2019
GNo G1801235
Type Of Funding C3120 - Aust Philanthropy
Category 3120
UON Y

Hormonal control of ovarian cancer$20,000

Funding body: Hunter Medical Research Institute

Funding body Hunter Medical Research Institute
Project Team Associate Professor Pradeep Tanwar, Ms Janine Lombard, Doctor Hiren Mandaliya, Mr Manish Kumar Jhamb, Doctor Muhammad Fairuz Jamaluddin
Scheme Project Grant
Role Investigator
Funding Start 2018
Funding Finish 2018
GNo G1801351
Type Of Funding C3120 - Aust Philanthropy
Category 3120
UON Y

Periostin as a biomarker in the diagnosis and surveillance of uterine leiomyomas$17,307

Funding body: John Hunter Hospital Charitable Trust

Funding body John Hunter Hospital Charitable Trust
Project Team Doctor Muhammad Fairuz Jamaluddin, Associate Professor Pradeep Tanwar, Doctor Pravin Nahar
Scheme Research Grant
Role Lead
Funding Start 2018
Funding Finish 2018
GNo G1800008
Type Of Funding C3112 - Aust Not for profit
Category 3112
UON Y

20171 grants / $20,000

Mediator complex subunit 12 (MED12) gene in pathogenesis of uterine smooth muscle tumours$20,000

Funding body: John Hunter Hospital Charitable Trust

Funding body John Hunter Hospital Charitable Trust
Project Team Doctor Muhammad Fairuz Jamaluddin, Associate Professor Pradeep Tanwar, Doctor Pravin Nahar
Scheme Research Grant
Role Lead
Funding Start 2017
Funding Finish 2017
GNo G1700368
Type Of Funding C3112 - Aust Not for profit
Category 3112
UON Y
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Research Supervision

Number of supervisions

Completed0
Current1

Current Supervision

Commenced Level of Study Research Title Program Supervisor Type
2020 PhD Developing Patient-Derived Ovarian Cancer Organoids as a Model for High Throughput Drug Screening and Personalised Medicine PhD (Medical Biochemistry), Faculty of Health and Medicine, The University of Newcastle Co-Supervisor
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Dr Muhammad Fairuz Jamaluddin

Position

Research Assistant
School of Biomedical Sciences and Pharmacy
Faculty of Health and Medicine

Contact Details

Email muhammad.jamaluddin@newcastle.edu.au
Phone (02) 4921 7476
Links Research Networks
Google+
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